The name's bond.......disulfide bond

Heras, Begona, Kurz, Mareike, Shouldice, Stephen R. and Martin, Jennifer L. (2007) The name's bond.......disulfide bond. Current Opinion in Structural Biology, 17 6: 691-698. doi:10.1016/

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Author Heras, Begona
Kurz, Mareike
Shouldice, Stephen R.
Martin, Jennifer L.
Title The name's bond.......disulfide bond
Journal name Current Opinion in Structural Biology   Check publisher's open access policy
ISSN 0959-440X
Publication date 2007-12
Sub-type Article (original research)
DOI 10.1016/
Open Access Status File (Author Post-print)
Volume 17
Issue 6
Start page 691
End page 698
Total pages 8
Place of publication London
Publisher Elsevier, Current Biology, LTD
Collection year 2008
Language eng
Subject 270199 Biochemistry and Cell Biology not elsewhere classified
780105 Biological sciences
Abstract A repeating theme in the structural biology of disulfide oxidants and isomerases is the extraordinary architectural similarity between functionally related proteins from prokaryotes and eukaryotes. The recently determined structure of full-length yeast protein disulfide isomerase (PDI) reveals a U-shaped molecule with two redox-active sites. It bears a remarkable resemblance to the V-shaped, but dimeric, bacterial disulfide isomerases DsbC and DsbG. Similarly, the much-anticipated structure of the bacterial membrane protein DsbB, the redox partner of DsbA, comprises a flexible redox loop embedded in an antiparallel four-helix bundle. This architecture is similar to that of soluble eukaryotic Ero1p and Erv2p proteins, the redox partners of PDI. Importantly, the DsbB crystal structure is a complex with DsbA, providing our first view of the molecular interactions between these two proteins.
Keyword Redox
protein disulfide isomerase
yeast protein
membrane protein
remarkable resemblance
prokaryotes and eukaryotes
s r Martin
Q-Index Code C1
Q-Index Status Confirmed Code

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Created: Tue, 22 Apr 2008, 10:35:33 EST by Cody Mudgway on behalf of Institute for Molecular Bioscience